The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p.
The structure of the two N-terminal domains of the gene 3 protein of filamentous phages (residues 1-217) has been solved by multiwavelength anomalous diffraction and refined at 1.46 A resolution. Each domain consists of either five or eight beta-strands and a single alpha-helix. Despite missing sequence homology, their cores superimposed with a root-mean-square deviation of 2 A. The domains are engaged in extensive interactions, resulting in a horseshoe shape with aliphatic amino acids and threonines lining the inside, delineating the likely binding site for the F-pilus. The glycine-rich linker connecting the domains is invisible in the otherwise highly ordered structure and may confer flexibility between the domains required during the infection process.
Lubkowski
J
J
Macromolecular Structure Laboratory, ABL-Basic Research Program, NCI-FCRDC, Frederick, Maryland 21702, USA.
Hennecke
F
F
Plückthun
A
A
Wlodawer
A
A
D000595:Amino Acid Sequence; D036022:Capsid Proteins; D018360:Crystallography, X-Ray / Q000379:methods*; D004268:DNA-Binding Proteins / Q000737:chemistry*; D017912:Inovirus / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019151:Peptide Library; D011487:Protein Conformation; D012645:Selenomethionine; D017386:Sequence Homology, Amino Acid; D014760:Viral Fusion Proteins / Q000737:chemistry*
D036022:Capsid Proteins; D004268:DNA-Binding Proteins; D019151:Peptide Library; D014760:Viral Fusion Proteins; D012645:Selenomethionine